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{{split}}
{{Pfam box
{{Pfam_box
| Symbol = cat
| Name = Catalase
| Name = Catalase
| image =
| Symbol = Catalase
| image = PDB 7cat EBI.jpg
| width =
| width =
| caption =
| caption =
Line 12: Line 11:
| SCOP = 7cat
| SCOP = 7cat
| TCDB =
| TCDB =
| CDD = cd00328
| OPM family = 370
| OPM protein = 3e4w
| PDB =
}}
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{enzyme
{{GNF_Protein_box
| Name = Catalase
| image = PBB_Protein_CAT_image.jpg
| EC_number = 1.11.1.6
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1dgb.
| CAS_number = 9001-05-2
| PDB = {{PDB2|1dgb}}, {{PDB2|1dgf}}, {{PDB2|1dgg}}, {{PDB2|1dgh}}, {{PDB2|1f4j}}, {{PDB2|1qqw}}, {{PDB2|1tgu}}, {{PDB2|1th2}}, {{PDB2|1th3}}, {{PDB2|1th4}}, {{PDB2|4blc}}, {{PDB2|7cat}}, {{PDB2|8cat}}
| IUBMB_EC_number = 1/11/1/6
| Name = Catalase
| GO_code = 0004096
| HGNCid = 1516
| image =
| Symbol = CAT
| width =
| AltSymbols =; MGC138422; MGC138424
| caption =
| OMIM = 115500
| ECnumber =  1.11.1.6
| Homologene = 55514
| MGIid = 88271
| GeneAtlas_image1 = PBB_GE_CAT_201432_at_tn.png
| GeneAtlas_image2 = PBB_GE_CAT_211922_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004096 |text = catalase activity}} {{GNF_GO|id=GO:0005506 |text = iron ion binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005777 |text = peroxisome}} {{GNF_GO|id=GO:0005778 |text = peroxisomal membrane}}
| Process = {{GNF_GO|id=GO:0006118 |text = electron transport}} {{GNF_GO|id=GO:0006979 |text = response to oxidative stress}} {{GNF_GO|id=GO:0042744 |text = hydrogen peroxide catabolic process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 847
    | Hs_Ensembl = ENSG00000121691
    | Hs_RefseqProtein = NP_001743
    | Hs_RefseqmRNA = NM_001752
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 11
    | Hs_GenLoc_start = 34417054
    | Hs_GenLoc_end = 34450176
    | Hs_Uniprot = P04040
    | Mm_EntrezGene = 12359
    | Mm_Ensembl = ENSMUSG00000027187
    | Mm_RefseqmRNA = NM_009804
    | Mm_RefseqProtein = NP_033934
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 2
    | Mm_GenLoc_start = 103254746
    | Mm_GenLoc_end = 103285962
    | Mm_Uniprot = Q3TVZ1
  }}
}}
}}
{{Infobox_gene}}
'''Catalase''' is a common [[enzyme]] found in nearly all living organisms exposed to oxygen (such as [[bacteria]], plants, and animals). It [[catalyst|catalyzes]] the decomposition of [[hydrogen peroxide]] to [[water]] and [[oxygen]].<ref name="pmid14745498">{{cite journal | vauthors = Chelikani P, Fita I, Loewen PC | title = Diversity of structures and properties among catalases | journal = Cellular and Molecular Life Sciences | volume = 61 | issue = 2 | pages = 192–208 | date = January 2004 | pmid = 14745498 | doi = 10.1007/s00018-003-3206-5 | url = }}</ref> It is a very important enzyme in protecting the cell from [[oxidative stress|oxidative damage]] by [[reactive oxygen species]] (ROS). Likewise, catalase has one of the highest [[turnover number]]s of all enzymes; one catalase molecule can convert millions of hydrogen peroxide molecules to water and oxygen each second.<ref>{{cite web | title = Catalase | author = Goodsell DS | work = Molecule of the Month | publisher = RCSB Protein Data Bank | url = http://pdb101.rcsb.org/motm/57 | date = 2004-09-01 | accessdate = 2016-08-23}}</ref>
Catalase is a [[Tetrameric protein|tetramer]] of four polypeptide chains, each over 500 [[amino acid]]s long.<ref name=Boon_a>{{cite web |vauthors=Boon EM, Downs A, Marcey D |title = Catalase: H<sub>2</sub>O<sub>2</sub>: H<sub>2</sub>O<sub>2</sub> Oxidoreductase | work = Catalase Structural Tutorial Text | url = http://biology.kenyon.edu/BMB/Chime/catalase/frames/cattx.htm | accessdate = 2007-02-11}}</ref> It contains four iron-containing [[heme]] groups that allow the enzyme to react with the hydrogen peroxide. The optimum [[pH]] for human catalase is approximately 7,<ref name="Maehly_1954">{{cite journal | vauthors = Maehly AC, Chance B | title = The assay of catalases and peroxidases | journal = Methods of Biochemical Analysis | volume = 1 | pages = 357–424 | year = 1954 | pmid = 13193536 | doi = 10.1002/9780470110171.ch14 | isbn = 978-0-470-11017-1 | series = Methods of Biochemical Analysis }}</ref> and has a fairly broad maximum: the rate of reaction does not change appreciably between pH 6.8 and 7.5.<ref name="pmid6727660">{{cite journal | vauthors = Aebi H | title = Catalase in vitro | journal = Methods in Enzymology | volume = 105 | pages = 121–6 | year = 1984 | pmid = 6727660 | doi = 10.1016/S0076-6879(84)05016-3 | isbn = 978-0-12-182005-3 | series = Methods in Enzymology }}</ref> The pH optimum for other catalases varies between 4 and 11 depending on the species.<ref name="urlEC 1.11.1.6 - catalase">{{cite web | url = http://www.brenda-enzymes.org/php/result_flat.php4?ecno=1.11.1.6&Suchword=&organism%5B%5D=&show_tm=0 | title = EC 1.11.1.6 - catalase | format = | work = BRENDA: The Comprehensive Enzyme Information System | publisher = Department of Bioinformatics and Biochemistry, Technische Universität Braunschweig | accessdate = 2009-05-26}}</ref> The optimum temperature also varies by species.<ref name=Bucknell>{{cite web | title = A Quantitative Enzyme Study; CATALASE |vauthors=Toner K, Sojka G, Ellis R | work = | publisher = bucknell.edu | url = http://www.facstaff.bucknell.edu/toner/gb/lab121/labs34.html | accessdate = 2007-02-11 |archiveurl = https://web.archive.org/web/20000612104029/http://www.facstaff.bucknell.edu/toner/gb/lab121/labs34.html |archivedate = 2000-06-12}}</ref>


{{SI}}
== Structure ==
Human catalase forms a [[tetramer]] composed of four [[Protein subunit|subunits]], each of which can be conceptually divided into four domains.<ref name = "Putnam_2000" >{{cite journal | vauthors = Putnam CD, Arvai AS, Bourne Y, Tainer JA | title = Active and inhibited human catalase structures: ligand and NADPH binding and catalytic mechanism | journal = Journal of Molecular Biology | volume = 296 | issue = 1 | pages = 295–309 | date = February 2000 | pmid = 10656833 | doi = 10.1006/jmbi.1999.3458 }}</ref> The extensive core of each subunit is generated by an eight-stranded antiparallel [[Beta barrel|b-barrel]] (b1-8), with nearest neighbor connectivity capped by b-barrel loops on one side and a9 loops on the other.<ref name = "Putnam_2000"  /> A [[Alpha helix|helical]] domain at one face of the b-barrel is composed of four C-terminal helices (a16, a17, a18, and a19) and four helices derived from residues between b4 and b5 (a4, a5, a6, and a7).<ref name = "Putnam_2000"  /> Alternative splicing may result in different protein variants.


{{CMG}}
== History ==
Catalase was not noticed until 1818 when [[Louis Jacques Thénard]], who discovered H<sub>2</sub>O<sub>2</sub> ([[hydrogen peroxide]]), suggested its breakdown is caused by an unknown substance. In 1900, [[Oscar Loew]] was the first to give it the name catalase, and found it in many plants and animals.<ref name="pmid17751716">{{cite journal | vauthors = Loew O | title =A New Enzyme of General Occurrence in Organisms | journal = Science | volume = 11 | issue = 279 | pages = 701–2 | date = May 1900 | pmid = 17751716 | doi = 10.1126/science.11.279.701 | bibcode = 1900Sci....11..701L | jstor = 1625707 }}</ref> In 1937 catalase from beef liver was crystallised by [[James B. Sumner]] and [[Alexander Dounce]]<ref name="pmid17776781">{{cite journal | vauthors = Sumner JB, Dounce AL | title = Crystalline Catalase | journal = Science | volume = 85 | issue = 2206 | pages = 366–7 | date = April 1937 | pmid = 17776781 | doi = 10.1126/science.85.2206.366 | bibcode = 1937Sci....85..366S }}</ref> and the molecular weight was found in 1938.<ref name="pmid17831682">{{cite journal | vauthors = Sumner JB, Gralén N | title = The Molecular Weight Of Crystalline Catalase | journal = Science | volume = 87 | issue = 2256 | pages = 284 | date = March 1938 | pmid = 17831682 | doi = 10.1126/science.87.2256.284 | bibcode = 1938Sci....87..284S }}</ref>


{{EH}}
The [[amino acid]] sequence of [[bovine]] catalase was determined in 1969,<ref name="pmid4892021">{{cite journal | vauthors = Schroeder WA, Shelton JR, Shelton JB, Robberson B, Apell G | title = The amino acid sequence of bovine liver catalase: a preliminary report | journal = Archives of Biochemistry and Biophysics | volume = 131 | issue = 2 | pages = 653–5 | date = May 1969 | pmid = 4892021 | doi = 10.1016/0003-9861(69)90441-X }}</ref> and the three-dimensional structure in 1981.<ref name="pmid7328661">{{cite journal | vauthors = Murthy MR, Reid TJ, Sicignano A, Tanaka N, Rossmann MG | title = Structure of beef liver catalase | journal = Journal of Molecular Biology | volume = 152 | issue = 2 | pages = 465–99 | date = October 1981 | pmid = 7328661 | doi = 10.1016/0022-2836(81)90254-0 }}</ref>


==Overview==
== Function ==
'''Catalase''' is a common [[enzyme]] found in nearly all living organisms. Its functions include [[catalyst|catalyzing]] the decomposition of [[hydrogen peroxide]] to [[water]] and [[oxygen]].<ref name=UAH_1>{{cite web | title = Catalase: An Enzyme at Work| work = Science Education Outreach | url=http://crystal.uah.edu/~carter/enzyme/catalase.htm | accessdate=2007-02-11}}</ref> Catalase has one of the highest turnover rates of all enzymes; one molecule of catalase can convert millions of molecules of hydrogen peroxide to water and oxygen per second.<ref>{{cite web | title = Catalase | work = Molecule of the Month | publisher = RCSB Protein Data Bank | url = http://www.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb57_1.html | date = 2004-09-01 | accessdate = 2007-02-11}}</ref>


Catalase is a [[tetramer]] of four polypeptide chains, each over 500 amino acids long.<ref name=Boon_a>{{cite web | author = Boon EM, Downs A, Marcey D |title = Catalase: H<sub>2</sub>O<sub>2</sub>: H<sub>2</sub>O<sub>2</sub> Oxidoreductase | work = Catalase Structural Tutorial Text | url = http://biology.kenyon.edu/BMB/Chime/catalase/frames/cattx.htm | accessdate = 2007-02-11}}</ref> It contains four [[porphyrin]] [[heme]] (iron) groups that allow the enzyme to react with the hydrogen peroxide. The optimum [[pH]] for catalase is approximately (pH 7.0),<ref name=Maehly_1954>{{cite book | authors = Maehly A, Chance B | title = The Assay of Catalases and Peroxidases ''in'' Methods of Biochemical Analysis | pages = 357 | year = 1954 | id = ISBN }}</ref> while the optimum temperature varies by species.<ref name=Bucknell>{{cite web | title = A Quantitative Enzyme Study; CATALASE | url = http://web.archive.org/web/20000612104029/http://www.facstaff.bucknell.edu/toner/gb/lab121/labs34.html | accessdate = 2007-02-11}}</ref>
=== Reaction ===
: 2 H<sub>2</sub>O<sub>2</sub> → 2 H<sub>2</sub>O + O<sub>2</sub>
 
The presence of catalase in a microbial or tissue sample can be demonstrated by adding [[hydrogen peroxide]] and observing the reaction. The production of [[oxygen]] can be seen by the formation of bubbles. This easy test, which can be seen with the naked eye, without the aid of instruments, is possible because catalase has a very high [[Enzyme assay#Specific activity|specific activity]], which produces a detectable response, as well as the fact that one of the products is a gas.
 
=== Molecular mechanism ===
While the complete mechanism of catalase is not currently known,<ref name=Boon_b/> the [[chemical reaction|reaction]] is believed to occur in two stages:
 
: H<sub>2</sub>O<sub>2</sub> + Fe(III)-E → H<sub>2</sub>O + O=Fe(IV)-E(.+)


==History==
: H<sub>2</sub>O<sub>2</sub> + O=Fe(IV)-E(.+) → H<sub>2</sub>O + Fe(III)-E + O<sub>2</sub><ref name=Boon_b>{{cite web |vauthors=Boon EM, Downs A, Marcey D | title = Proposed Mechanism of Catalase | work = Catalase: H<sub>2</sub>O<sub>2</sub>: H<sub>2</sub>O<sub>2</sub> Oxidoreductase: Catalase Structural Tutorial | url = http://biology.kenyon.edu/BMB/Chime/catalase/frames/cattx.htm#Proposed%20Mechanism%20of%20Catalase | accessdate = 2007-02-11}}</ref>
Catalase was first noticed as a substance in [[1811]] when [[Louis Jacques Thénard]], who discovered H<sub>2</sub>O<sub>2</sub> (hydrogen peroxide), suggested that its breakdown is caused by a substance.


In [[1900]] [[Oscar Loew]] was the first to give it the name catalase, and found its presence in many plants and animals<ref>{{cite journal
Here Fe()-E represents the [[iron]] center of the [[heme]] group attached to the enzyme. Fe(IV)-E(.+) is a mesomeric form of Fe(V)-E, meaning the iron is not completely oxidized to +V, but receives some stabilising electron density from the heme ligand, which is then shown as a radical cation (.+).
|title=A New Enzyme of General Occurrence in Organisms
|author=Loew, Oscar
|journal=Science
|volume=11
|issue=279
|pages=701-2
|month=May
|year=1900
| doi = 10.1126/science.11.279.701 <!--Retrieved from CrossRef by DOI bot-->
}}</ref>. In [[1937]] catalase from beef liver was crystallised by [[James B. Sumner]] <ref>{{cite journal
|journal=Science
|title=Cystalline Catalase
|author=Sumner, J.B.
|authorlink=James B. Sumner
|coauthors=Dounce, A. L.
|volume=87
|issue=18
|year=1938 | pages = 284
| doi = 10.1126/science.87.2256.284 <!--Retrieved from CrossRef by DOI bot-->
}}</ref> and the molecular weight worked out in [[1938]]<ref>{{cite journal
|title=The Molecular Weight of Crystalline Catalase
|author=Sumner, James B.
|coauthors=Gralen, Nils
|journal=Science
|volume=87
|issue=2256
|pages=284
|month=Mar fart
|year=1938 | doi = 10.1126/science.87.2256.284 <!--Retrieved from CrossRef by DOI bot-->
}}</ref>.
In [[1969]] the [[amino acid]] sequence of [[bovine]] catalase was worked out<ref>{{cite journal
|author=Schroeder WA
|coauthors=Shelton JR; Shelton JB; Robberson B; Apell G.
|title=The amino acid sequence of bovine liver catalase: a preliminary report.
|journal=Arch Biochem Biophys
|year=1969
|month=May
|volume=131|issue=2|pages=653-5
|pmid=4892021
| doi = 10.1016/0003-9861(69)90441-X <!--Retrieved from CrossRef by DOI bot-->
}}</ref>. Then in [[1981]], the 3D structure of the protein was revealed<ref>{{cite journal
|title=Structure of beef liver catalase.
|author=Murthy MR
|coauthors=Reid TJ 3rd; Sicignano A; Tanaka N; Rossmann MG.
|journal=J Mol Biol
|year=1981
|month=Oct
|volume=152|issue=2|pages=465-99
|pmid=7328661
| doi = 10.1016/0022-2836(81)90254-0 <!--Retrieved from CrossRef by DOI bot-->
}}</ref>.


==Action of catalase==
As hydrogen peroxide enters the [[active site]], it interacts with the [[amino acid]]s Asn148 ([[asparagine]] at position 148) and [[histidine|His75]], causing a [[proton]] (hydrogen [[ion]]) to transfer between the oxygen atoms. The free oxygen atom coordinates, freeing the newly formed water molecule and Fe(IV)=O. Fe(IV)=O reacts with a second hydrogen peroxide molecule to reform Fe(III)-E and produce water and oxygen.<ref name=Boon_b /> The reactivity of the iron center may be improved by the presence of the phenolate [[ligand]] of [[tyrosine|Tyr358]] in the fifth coordination position, which can assist in the [[oxidation]] of the Fe(III) to Fe(IV). The efficiency of the reaction may also be improved by the interactions of His75 and Asn148 with [[reaction intermediates]].<ref name=Boon_b /> In general, the rate of the reaction can be determined by the [[Michaelis–Menten kinetics|Michaelis-Menten equation]].<ref name="urlRe: How does the concentration of hydrogen peroxide affect the reaction...">{{cite web | url = http://www.madsci.org/posts/archives/aug98/900981784.Bc.r.html | title = How does the concentration of hydrogen peroxide affect the reaction | author = Maass E | date = 1998-07-19 | work = | publisher = MadSci Network | accessdate = 2009-03-02 }}</ref>
The reaction of catalase in the decomposition of hydrogen peroxide is:


: 2 H<sub>2</sub>O<sub>2</sub> → 2 H<sub>2</sub>O + O<sub>2</sub><ref name=UAH_2>{{cite web | title = Catalase: A Closer Look | work = Science Education Outreach | url=http://crystal.uah.edu/~carter/enzyme/closer.htm | accessdate=2007-02-11}}</ref>
Catalase can also catalyze the oxidation, by [[hydrogen peroxide]], of various metabolites and toxins, including [[formaldehyde]], [[formic acid]], [[phenols]], [[acetaldehyde]] and [[alcohols]]. It does so according to the following reaction:


In [[microbiology]], the ''catalase test'' is used to differentiate between [[bacteria]]l [[species]] in the lab.[http://www2.austin.cc.tx.us/microbugz/html/catalase_test.html] The test is done by placing a drop of hydrogen peroxide on a [[microscope slide]]. Using an applicator stick, a scientist touches the colony and then smears a sample into the hydrogen peroxide drop. If bubbles or froth forms, the organism is said to be ''catalase-positive''; if not, the organism is ''catalase-negative''.[http://dentistry.ouhsc.edu/intranet-web/courses/dmi_8351/Catalase.html] This test is particularly useful in distinguishing [[staphylococcus|staphylococci]] and [[micrococcus|micrococci]], which are catalase-positive, from [[streptococcus|streptococci]] and [[enterococcus|enterococci]], which are catalase-negative.[http://www2.austin.cc.tx.us/microbugz/html/catalase_test.html] While the catalase test alone cannot identify a particular organism, combined with other tests, it can aid diagnosis. The presence of catalase in bacterial cells depends on both the growth condition and the medium used to grow the cells.
: H<sub>2</sub>O<sub>2</sub> + H<sub>2</sub>R → 2H<sub>2</sub>O + R


==Molecular mechanism==
The exact mechanism of this reaction is not known.
While the complete mechanism of catalase is not currently known, the [[chemical reaction|reaction]] is believed to occur in two stages:


: H<sub>2</sub>O<sub>2</sub> + Fe(III)-E → H<sub>2</sub>O + O=Fe(IV)-E(.+)
Any heavy metal ion (such as copper cations in [[copper(II) sulfate]]) can act as a [[noncompetitive inhibitor]] of catalase. Furthermore, the poison [[cyanide]] is a noncompetitive inhibitor<ref>Nonstationary Inhibition of Enzyme Action. The Cyanide Inhibition of Catalase</ref> of catalase at high concentrations of [[hydrogen peroxide]].<ref>{{cite journal | vauthors = Ogura Y, Yamazaki I | title = Steady-state kinetics of the catalase reaction in the presence of cyanide | journal = Journal of Biochemistry | volume = 94 | issue = 2 | pages = 403–8 | date = August 1983 | pmid = 6630165 | doi =  10.1093/oxfordjournals.jbchem.a134369}}</ref>
[[Arsenate]] acts as an [[Enzyme activator|activator]].<ref>{{cite journal | vauthors = Kertulis-Tartar GM, Rathinasabapathi B, Ma LQ | title = Characterization of glutathione reductase and catalase in the fronds of two Pteris ferns upon arsenic exposure | journal = Plant Physiology and Biochemistry | volume = 47 | issue = 10 | pages = 960–5 | date = October 2009 | pmid = 19574057 | doi = 10.1016/j.plaphy.2009.05.009 }}</ref> Three-dimensional [[protein structure]]s of the peroxidated catalase intermediates are available at the [[Protein Data Bank]].


: H<sub>2</sub>O<sub>2</sub> + O=Fe(IV)-E(.+) → H<sub>2</sub>O + Fe(III)-E + O<sub>2</sub><ref name=Boon_b>{{cite web | author = Boon EM, Downs A, Marcey D | title = Proposed Mechanism of Catalase ''in'' Catalase: H<sub>2</sub>O<sub>2</sub>: H<sub>2</sub>O<sub>2</sub> Oxidoreductase | work = Catalase Structural Tutorial Text | url = http://biology.kenyon.edu/BMB/Chime/catalase/frames/cattx.htm#Proposed%20Mechanism%20of%20Catalase | accessdate = 2007-02-11}}</ref>
=== Cellular role ===
Hydrogen peroxide is a harmful byproduct of many normal [[metabolism|metabolic]] processes; to prevent damage to cells and tissues, it must be quickly converted into other, less dangerous substances. To this end, catalase is frequently used by cells to rapidly catalyze the [[Chemical decomposition|decomposition]] of hydrogen peroxide into less-reactive [[gas]]eous [[oxygen]] and water molecules.<ref name=Gaetani_1996>{{cite journal | vauthors = Gaetani GF, Ferraris AM, Rolfo M, Mangerini R, Arena S, Kirkman HN | title = Predominant role of catalase in the disposal of hydrogen peroxide within human erythrocytes | journal = Blood | volume = 87 | issue = 4 | pages = 1595–9 | date = February 1996 | pmid = 8608252 }}</ref>


:Here Fe()-E represents the [[iron]] centre of the [[heme]] group attached to the enzyme. Fe(IV)-E(.+) ís a mesomeric form of Fe(V)-E, meaning that iron is not completely oxidized to +V but receives some "supporting electron" from the heme ligand. This heme has to be drawn then als radical cation (.+).
Mice genetically engineered to lack catalase are initially phenotypically normal.,<ref name=Ho_2004>{{cite journal | vauthors = Ho YS, Xiong Y, Ma W, Spector A, Ho DS | title = Mice lacking catalase develop normally but show differential sensitivity to oxidant tissue injury | journal = The Journal of Biological Chemistry | volume = 279 | issue = 31 | pages = 32804–12 | date = July 2004 | pmid = 15178682 | doi = 10.1074/jbc.M404800200 }}</ref> however, catalase deficiency in mice may increase the likelihood of developing [[obesity]], fatty liver,<ref name="pmid27939935">{{cite journal | vauthors = Heit C, Marshall S, Singh S, Yu X, Charkoftaki G, Zhao H, Orlicky DJ, Fritz KS, Thompson DC, Vasiliou V | title = Catalase deletion promotes prediabetic phenotype in mice | journal = Free Radical Biology & Medicine | volume = 103 | issue = | pages = 48–56 | year = 2017 | pmid = 27939935 | doi = 10.1016/j.freeradbiomed.2016.12.011 | pmc=5513671}}</ref> and [[Diabetes mellitus type 2|type 2 diabetes]].<ref name="Góth_2012">{{cite journal | vauthors = Góth L, Nagy T | title = Acatalasemia and diabetes mellitus | journal = Archives of Biochemistry and Biophysics | volume = 525 | issue = 2 | pages = 195–200 | year = 2012 | pmid = 22365890 | doi = 10.1016/j.abb.2012.02.005 }}</ref> Some humans have very low levels of catalase ([[acatalasia]]), yet show few ill effects.


As hydrogen peroxide enters the [[active site]], it interacts with the [[amino acid]]s Asn147 ([[asparagine]] at position 147) and [[histidine|His74]], causing a [[proton]] (hydrogen [[ion]]) to transfer between the oxygen atoms. The free oxygen atom coordinates, freeing the newly-formed water molecule and Fe(IV)=O. Fe(IV)=O reacts with a second hydrogen peroxide molecule to reform Fe(III)-E and produce water and oxygen.<ref name=Boon_b /> The reactivity of the iron center may be improved by the presence of the phenolate [[ligand]] of [[tyrosine|Tyr357]] in the fifth iron [[ligand]], which can assist in the [[oxidation]] of the Fe(III) to Fe(IV). The efficiency of the reaction may also be improved by the interactions of His74 and Asn147 with [[reaction intermediates]].<ref name=Boon_b /> In general, the rate of the reaction can be determined by the [[Michaelis-Menten equation]].[http://www.madsci.org/posts/archives/aug98/900981784.Bc.r.html]
The increased [[oxidative stress]] that occurs with [[ageing|aging]] in mice is alleviated by [[gene expression|over-expression]] of catalase.<ref name="pmid27575890">{{cite journal |vauthors=Selvaratnam J, Robaire B |title=Overexpression of catalase in mice reduces age-related oxidative stress and maintains sperm production |journal=Exp. Gerontol. |volume=84 |issue= |pages=12–20 |date=November 2016 |pmid=27575890 |doi=10.1016/j.exger.2016.08.012 |url=}}</ref> Over-expressing mice do not exhibit the age-associated loss of [[spermatozoon|spermatozoa]], [[testicle|testicular]] [[germ cell|germ]] and [[Sertoli cell]]s seen in wild-type mice.  Oxidative stress in [[wild-type]] mice ordinarily induces oxidative [[DNA damage (naturally occurring)|DNA damage]] (measured as [[8-Oxo-2'-deoxyguanosine|8-oxodG]]) in [[sperm]] with aging, but these damages are significantly reduced in aged catalase over-expressing mice.<ref name="pmid27575890" />   Furthermore, these over-expressing mice show no decrease in age-dependent number of pups per litter.  Overexpression of catalase targeted to mitochondria extends the lifespan of mice.<ref name="pmid15879174">{{cite journal |vauthors=Schriner SE, Linford NJ, Martin GM, Treuting P, Ogburn CE, Emond M, Coskun PE, Ladiges W, Wolf N, Van Remmen H, Wallace DC, Rabinovitch PS |title=Extension of murine life span by overexpression of catalase targeted to mitochondria |journal=Science |volume=308 |issue=5730 |pages=1909–11 |date=June 2005 |pmid=15879174 |doi=10.1126/science.1106653 |url=|bibcode=2005Sci...308.1909S }}</ref>


Catalase can also oxidize different toxins, such as [[formaldehyde]], [[formic acid]], and [[alcohols]]. In doing so, it uses [[hydrogen peroxide]] according to the following reaction:
Catalase is usually located in a cellular [[organelle]] called the [[peroxisome]].<ref name="MBOC">{{cite book |vauthors=Alberts B, Johnson A, Lewis J, Raff M, Roberts K, Walter P | title = Molecular Biology of the Cell | edition = 4th | publisher = Garland Science | location = New York | year = 2002 | origyear = | pages = | chapter = Peroxisomes | chapterurl = https://www.ncbi.nlm.nih.gov/books/NBK26858/ | quote = | isbn = 978-0-8153-3218-3 }}</ref> Peroxisomes in plant cells are involved in [[photorespiration]] (the use of oxygen and production of carbon dioxide) and symbiotic [[nitrogen fixation]] (the breaking apart of [[diatomic]] [[nitrogen]] (N<sub>2</sub>) to reactive nitrogen atoms). Hydrogen peroxide is used as a potent antimicrobial agent when cells are infected with a pathogen. Catalase-positive pathogens, such as ''[[Mycobacterium tuberculosis]]'', ''[[Legionella pneumophila]]'', and ''[[Campylobacter jejuni]]'', make catalase to deactivate the peroxide radicals, thus allowing them to survive unharmed within the [[Host (biology)|host]].<ref name="pmid12949187">{{cite journal | vauthors = Srinivasa Rao PS, Yamada Y, Leung KY | title = A major catalase (KatB) that is required for resistance to H2O2 and phagocyte-mediated killing in Edwardsiella tarda | journal = Microbiology | volume = 149 | issue = Pt 9 | pages = 2635–44 | date = September 2003 | pmid = 12949187 | doi = 10.1099/mic.0.26478-0 }}</ref>


: H<sub>2</sub>O<sub>2</sub> + H<sub>2</sub>R → 2H<sub>2</sub>O + R
Like [[alcohol dehydrogenase]], catalase converts ethanol to acetaldehyde, but it is unlikely that this reaction is physiologically significant.<ref name="lieb97">{{cite journal|last1=Lieber|first1=Charles S.|title=Ethanol metabolism, cirrhosis and alcoholism|journal=Clinica Chimica Acta|date=January 1997|volume=257|issue=1|pages=59–84|doi=10.1016/S0009-8981(96)06434-0}}</ref>


Again, the exact mechanism of this reaction is not known.
== Distribution among organisms ==
The large majority of known organisms use catalase in every [[organ (anatomy)|organ]], with particularly high concentrations occurring in the [[liver]] in mammals.<ref>{{cite journal| vauthors = Ilyukha VA | journal=Journal of Evolutionary Biochemistry and Physiology | title = Superoxide Dismutase and Catalase in the Organs of Mammals of Different Ecogenesis |date=2001|volume=37|issue=3|pages=241–245|doi=10.1023/A:1012663105999}}</ref>Almost all [[aerobic microorganisms]] use catalase. It is also present in some [[Anaerobic organism|anaerobic]] [[microorganisms]], such as ''[[Methanosarcina barkeri]]''.<ref name="pmid16735730">{{cite journal | vauthors = Brioukhanov AL, Netrusov AI, Eggen RI | title = The catalase and superoxide dismutase genes are transcriptionally up-regulated upon oxidative stress in the strictly anaerobic archaeon Methanosarcina barkeri | journal = Microbiology | volume = 152 | issue = Pt 6 | pages = 1671–7 | date = June 2006 | pmid = 16735730 | doi = 10.1099/mic.0.28542-0 }}</ref> Catalase is also universal among [[plants]] and occurs in most [[fungi]].<ref>{{cite journal | vauthors = Hansberg W, Salas-Lizana R, Domínguez L | title = Fungal catalases: function, phylogenetic origin and structure | journal = Archives of Biochemistry and Biophysics | volume = 525 | issue = 2 | pages = 170–80 | date = September 2012 | pmid = 22698962 | doi = 10.1016/j.abb.2012.05.014 }}</ref>


Any heavy metal ion (such as copper cations in [[copper(II) sulfate]]) will act as a [[noncompetitive inhibitor]] on catalase. Also, the poison [[cyanide]] is a [[competitive inhibitor]] of catalase, strongly binding to the [[heme]] of catalase and stopping the enzyme's action.
One unique use of catalase occurs in the [[bombardier beetle]]. This beetle has two sets of liquids that are stored separately in two paired glands. The larger of the pair, the storage chamber or reservoir, contains [[hydroquinone]]s and hydrogen peroxide, while the smaller, the reaction chamber, contains catalases and [[peroxidase]]s. To activate the noxious spray, the beetle mixes the contents of the two compartments, causing oxygen to be liberated from hydrogen peroxide. The oxygen oxidizes the hydroquinones and also acts as the propellant.<ref name="pmid10449758">{{cite journal|vauthors=Eisner T, Aneshansley DJ|date=August 1999|title=Spray aiming in the bombardier beetle: photographic evidence|journal=Proceedings of the National Academy of Sciences of the United States of America|volume=96|issue=17|pages=9705–9|bibcode=1999PNAS...96.9705E|doi=10.1073/pnas.96.17.9705|pmc=22274|pmid=10449758}}</ref> The oxidation reaction is very [[exothermic]] (ΔH = −202.8 kJ/mol) and rapidly heats the mixture to the boiling point.<ref name="Beheshti_2006">{{cite journal|vauthors=Beheshti N, McIntosh AC|year=2006|title=A biomimetic study of the explosive discharge of the bombardier beetle|url=http://www.heveliusforum.org/Artykuly/Biomimetics.pdf|deadurl=yes|journal=Int. Journal of Design & Nature|volume=1|issue=1|pages=1–9|archiveurl=https://web.archive.org/web/20110726145856/http://www.heveliusforum.org/Artykuly/Biomimetics.pdf|archivedate=2011-07-26}}</ref>


Three-dimensional [[protein structure]]s of the peroxidated catalase intermediates are available at the [[Protein Data Bank]]. This enzyme is commonly used in laboratories as a tool for learning the effect of enzymes upon reaction rates.
Long-lived queens of the [[termite]] ''[[Reticulitermes]] speratus'' have significantly lower [[DNA oxidation|oxidative damage to their DNA]] than non-reproductive individuals (workers and soldiers).<ref name="pmid28076409">{{cite journal |vauthors=Tasaki E, Kobayashi K, Matsuura K, Iuchi Y |title=An Efficient Antioxidant System in a Long-Lived Termite Queen |journal=PLoS ONE |volume=12 |issue=1 |pages=e0167412 |date=2017 |pmid=28076409 |pmc=5226355 |doi=10.1371/journal.pone.0167412 |url=|bibcode=2017PLoSO..1267412T }}</ref>  Queens have more than two times higher catalase activity and seven times higher expression levels of the catalase gene RsCAT1 than workers.<ref name="pmid28076409" />  It appears that the efficient [[antioxidant]] capability of termite queens can partly explain how they attain longer life.


==Cellular role==
Catalase enzymes from various species have vastly differing optimum temperatures. [[Poikilotherm]]ic animals typically have catalases with optimum temperatures in the range of 15-25&nbsp;°C, while mammalian or avian catalases might have optimum temperatures above 35&nbsp;°C,<ref name="mits56" /><ref name="imm03">{{cite journal|last1=Akkuş Çetinus|first1=Şenay|last2=Nursevin Öztop|first2=H. | name-list-format = vanc |title=Immobilization of catalase into chemically crosslinked chitosan beads|journal=Enzyme and Microbial Technology|date=June 2003|volume=32|issue=7|pages=889–894|doi=10.1016/S0141-0229(03)00065-6}}</ref> and catalases from plants vary depending on their [[growth habit]].<ref name="mits56">{{cite journal|last1=Mitsuda|first1=Hisateru|title=Studies on Catalase|journal=Bulletin of the Institute for Chemical Research, Kyoto University|date=1956-07-31|volume=34|issue=4|pages=165–192|url=https://repository.kulib.kyoto-u.ac.jp/dspace/bitstream/2433/75561/1/chd034_4_165.pdf|accessdate=27 September 2017}}</ref> In contrast, catalase isolated from the [[hyperthermophile]] [[archaeon]] ''[[Pyrobaculum calidifontis]]'' has a temperature optimum of 90&nbsp;°C.<ref name="pmid12029047">{{cite journal | vauthors = Amo T, Atomi H, Imanaka T | title = Unique presence of a manganese catalase in a hyperthermophilic archaeon, Pyrobaculum calidifontis VA1 | journal = Journal of Bacteriology | volume = 184 | issue = 12 | pages = 3305–12 | date = June 2002 | pmid = 12029047 | pmc = 135111 | doi = 10.1128/JB.184.12.3305-3312.2002 }}</ref>
Hydrogen peroxide is a harmful by-product of many normal [[metabolism|metabolic]] processes: To prevent damage, it must be quickly converted into other, less dangerous substances. To this end, catalase is frequently used by cells to rapidly catalyze the [[Chemical decomposition|decomposition]] of hydrogen peroxide into less reactive [[gas]]eous [[oxygen]] and water molecules.<ref name=Gaetani_1996>{{cite journal | author = Gaetani G, Ferraris A, Rolfo M, Mangerini R, Arena S, Kirkman H | title = Predominant role of catalase in the disposal of hydrogen peroxide within human erythrocytes. | journal = Blood | volume = 87 | issue = 4 | pages = 1595-9 | year = 1996 | id = PMID 8608252}}</ref>


The true biological significance of catalase is not always straightforward to assess: Mice genetically engineered to lack catalase are phenotypically normal, indicating that this enzyme is dispensable in animals under some conditions.<ref name=Ho_2004>{{cite journal | author = Ho YS, Xiong Y, Ma W, Spector A, Ho D | title = Mice Lacking Catalase Develop Normally but Show Differential Sensitivity to Oxidant Tissue Injury. | journal = J Biol Chem | volume = 279 | issue = 31 | pages = 32804-812 | year = 2004 | id = PMID 15178682 | doi = 10.1074/jbc.M404800200 <!--Retrieved from CrossRef by DOI bot-->}}</ref>
== Clinical significance and application ==
[[Image:Hydrogen-peroxide-2D.png|left|thumb|Hydrogen peroxide]]
Catalase is used in the food industry for removing [[hydrogen peroxide]] from [[milk]] prior to [[cheese]] production.<ref name="urlCatalase - Worthington Enzyme Manual">{{cite web | url = http://www.worthington-biochem.com/CTL/default.html | title = Catalase | work = Worthington Enzyme Manual | publisher = Worthington Biochemical Corporation | accessdate = 2009-03-01}}</ref> Another use is in food wrappers where it prevents food from [[oxidation|oxidizing]].<ref name="urlRe: how is catalase used in industry?">{{cite web | url = http://madsci.org/posts/archives/mar99/921636249.Gb.r.html | title = Re: how is catalase used in industry? | author = Hengge A | date = 1999-03-16 | work = General Biology | publisher = MadSci Network | accessdate = 2009-03-01}}</ref> Catalase is also used in the [[textile]] industry, removing hydrogen peroxide from fabrics to make sure the material is peroxide-free.<ref name="urltextile industry">{{cite web | url = http://www.p2pays.org/ref/11/10842.htm | title = textile industry | work = Case study 228 | publisher = International Cleaner Production Information Clearinghouse | accessdate = 2009-03-01}}</ref>


Some human beings have very low levels of catalase ([[acatalesimia]]), yet show few ill effects. It is likely that the predominant scavengers of H2O2 in normal mammalian cells are [[preoxiredoxins]] rather than catalase.
A minor use is in [[contact lens]] hygiene – a few lens-cleaning products [[disinfection|disinfect]] the lens using a hydrogen peroxide solution; a solution containing catalase is then used to decompose the hydrogen peroxide before the lens is used again.<ref>{{US patent reference | number = 5521091 | y = 1996 | m = 05 | d = 28 | inventor = Cook JN, Worsley JL | title = Compositions and method for destroying hydrogen peroxide on contact lens }}</ref>


Catalase works at an optimum temperature of 37 °C, which is approximately the temperature of the human body.
=== Bacterial identification (catalase test) ===
[[Image:Catalase reaction.jpg|300px|thumb|Positive catalase reaction]]
The catalase test is one of the three main tests used by microbiologists to identify species of bacteria. If the bacteria possess catalase (i.e., are catalase-positive), when a small amount of bacterial [[Isolation (microbiology)|isolate]] is added to hydrogen peroxide, bubbles of oxygen are observed. The catalase test is done by placing a drop of hydrogen peroxide on a [[microscope slide]]. An applicator stick is touched to the colony, and the tip is then smeared onto the hydrogen peroxide drop.
* If the mixture produces bubbles or froth, the organism is said to be 'catalase-positive'. [[Staphylococcus|Staphylococci]]<ref name="urlBSCI 424 Pathogenic Microbiology -- Bacterial Pathogen List">{{cite web | url = http://www.life.umd.edu/classroom/bsci424/pathogendescriptions/PathogenList.htm | title = Bacterial Pathogen List | author = Rollins DM | date = 2000-08-01 | work = BSCI 424 Pathogenic Microbiology | publisher = University of Maryland | accessdate = 2009-03-01}}</ref> and [[Micrococcus|Micrococci]]<ref name="urlBiochemical Tests">{{cite web | url = http://www.mc.maricopa.edu/~johnson/labtools/Dbiochem/cat.html | title = Catalase Production | author = Johnson M | work = Biochemical Tests | publisher = Mesa Community College | accessdate = 2009-03-01 | deadurl = yes | archiveurl = https://web.archive.org/web/20081211073437/http://www.mc.maricopa.edu/~johnson/labtools/Dbiochem/cat.html | archivedate = 2008-12-11 | df =  }}</ref> are catalase-positive. Other catalase-positive organisms include ''[[Listeria]], [[Corynebacterium diphtheriae]], [[Burkholderia cepacia]], [[Nocardia]]'', the family Enterobacteriaceae (''[[Citrobacter]], [[Escherichia coli|E. coli]], [[Enterobacter]], [[Klebsiella]], [[Shigella]], [[Yersinia]], [[Proteus (bacterium)|Proteus]], [[Salmonella]], [[Serratia]]''), [[Pseudomonas]], ''[[Mycobacterium tuberculosis]], [[Aspergillus]]'', [[Cryptococcus (fungus)|''Cryptococcus'']], and ''[[Rhodococcus equi]]''.
* If not, the organism is 'catalase-negative'. ''[[Streptococcus]]''<ref name="urlStreptococcus pneumoniae and Staphylococci">{{cite web | url = http://pathmicro.med.sc.edu/fox/strep-staph.htm | title = Streptococcus pneumoniae and Staphylococci | author = Fox A | work = | publisher = University of South Carolina | accessdate = 2009-03-01}}</ref> and ''[[Enterococcus]]'' spp. are catalase-negative.


Catalase is usually located in a cellular [[organelle]] called the [[peroxisome]].<ref name=MBOC>{{cite book | author = Alberts B, Johnson A, Lewis J, Raff M, Roberts K, Walter P | title = Peroxisomes, ''in'' ''Molecular Biology of the Cell'' | edition = 4th ed. | publisher = Garland | year = 2002 | id = [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Search&db=books&doptcmdl=GenBookHL&term=catalase+AND+mboc4%5Bbook%5D+AND+373476%5Buid%5D&rid=mboc4.section.2194 (via NCBI Bookshelf)] ISBN 0815332181}}</ref> Peroxisomes in plant cells are involved in [[photorespiration]] (the use of oxygen and production of carbon dioxide) and symbiotic [[nitrogen fixation]] (the breaking apart of [[diatomic]] [[nitrogen]] (N<sub>2</sub>) to reactive nitrogen atoms).
While the catalase test alone cannot identify a particular organism, it can aid identification when combined with other tests such as antibiotic resistance. The presence of catalase in bacterial cells depends on both the growth condition and the medium used to grow the cells.


Hydrogen peroxide is used as a potent antimicrobial agent when cells are infected with a pathogen. Pathogens that are catalase-positive, such as ''[[Mycobacterium tuberculosis]]'', ''[[Legionella pneumophila]]'', and ''[[Campylobacter jejuni]]'', make catalase in order to deactivate the peroxide radicals, thus allowing them to survive unharmed within the [[Host (biology)|host ]].[http://mic.sgmjournals.org/cgi/content/full/149/9/2635]
[[Capillary tube]]s may also be used. A small sample of bacteria is collected on the end of the capillary tube, without blocking the tube, to avoid [[false negative]] results. The opposite end is then dipped into hydrogen peroxide, which is drawn into the tube through [[capillary action]], and turned upside down, so that the bacterial points downwards. The hand holding the tube is then tapped on the bench, moving the hydrogen peroxide down until it touches the bacteria. If bubbles form on contact, this indicates a positive catalase result. This test can detect catalase-positive bacteria at concentrations above about 10<sup>5</sup> cells/mL,<ref>{{Cite book|url=https://books.google.com/books?id=_orkBwAAQBAJ&pg=PA35|title=Fisheries Processing: Biotechnological applications|last=Martin|first=A. M.|date=2012-12-06|publisher=Springer Science & Business Media|isbn=9781461553038|language=en}}</ref> and is simple to use.


==Distribution among organisms==
=== Bacterial virulence ===
All known [[animals]] use catalase in every [[organ (anatomy)|organ]], with particularly high concentrations occurring in the [[liver]]. One unique use of catalase occurs in [[bombardier beetle]]. The beetle has two sets of chemicals ordinarily stored separately in its paired glands. The larger of the pair, the storage chamber or reservoir, contains [[hydroquinone]]s and [[hydrogen peroxide]], whereas the smaller of the pair, the reaction chamber, contains catalases and [[peroxidase]]s. To activate the spray, the beetle mixes the contents of the two compartments, causing oxygen to be liberated from hydrogen peroxide. The oxygen oxidizes the hydroquinones and also acts as the propellant. <REF>{{cite journal| pmid = 10449758 | title = Spray aiming in the bombardier beetle: photographic evidence. | author =     T Eisner and DJ Aneshansley | journal = Proc Natl Acad Sci U S A | date = 1999 Aug | volume = 96 | issue = 17 | pages = 9705-9}}</REF>  
[[Neutrophil]]s and other [[phagocyte]]s use peroxide to kill bacteria. The enzyme [[NADPH oxidase]] generates [[superoxide]] within the [[phagosome]], which is converted via hydrogen peroxide to other oxidising substances like [[hypochlorous acid]] which kill [[phagocytosed]] pathogens.<ref>{{Cite journal|last=Winterbourn|first=Christine C.|last2=Kettle|first2=Anthony J.|last3=Hampton|first3=Mark B.|date=2016-06-02|title=Reactive Oxygen Species and Neutrophil Function|url=http://www.annualreviews.org/doi/10.1146/annurev-biochem-060815-014442|journal=Annual Review of Biochemistry|volume=85|issue=1|pages=765–792|doi=10.1146/annurev-biochem-060815-014442|issn=0066-4154}}</ref> In individuals with [[chronic granulomatous disease]] (CGD) there is a defect in producing peroxide via mutations in phagocyte oxidases such as [[myeloperoxidase]].<ref>{{Cite book|url=https://books.google.com/books?id=1NzVBQAAQBAJ&pg=PA169|title=The Neutrophil|last=Murphy|first=Patrick|date=2012-12-06|publisher=Springer Science & Business Media|isbn=9781468474183|language=en}}</ref> Normal cellular metabolism will still produce a small amount of peroxide and this peroxide can be used to produce hypochlorous acid to eradicate the bacterial infection. However, if individuals with CGD are infected with catalase-positive bacteria, the bacterial catalase can destroy the excess peroxide before it can be used to produce other oxidising substances. In these individuals the pathogen survives and becomes a chronic infection. This chronic infection is typically surrounded by macrophages in an attempt to isolate the infection. This wall of macrophages surrounding a pathogen is called a [[granuloma]]. Many bacteria are catalase positive, but some are better catalase-producers than others. The mnemonic "cats Need PLACESS to Belch their Hairballs" can be used to memorise the catalase-positive bacteria: [[nocardia]], [[pseudomonas]], [[listeria]], [[aspergillus]], [[Candida albicans|candida]], [[Escherichia coli|E. coli]], [[staphylococcus]], [[serratia]], [[Burkholderia cepacia complex|B. cepacia]] and [[Helicobacter pylori|H. pylori]].<ref>{{Cite book|url=https://www.worldcat.org/oclc/986222844|title=First aid for the USMLE step 1 2017 : a student-to-student guide|others=Le, Tao,, Bhushan, Vikas,, Sochat, Matthew,, Kallianos, Kimberly,, Chavda, Yash,, Zureick, Andrew H. (Andrew Harrison), 1991-|isbn=9781259837623|edition=27th|location=New York|oclc=986222844}}</ref>


Catalase is also universal among [[plants]], but not among [[fungi]], although some species have been found to produce the enzyme when growing in an environment with a low pH and warm temperatures.<ref>{{cite journal| pmid = 16503295 | title = Production of catalase by fungi growing at low pH and high temperature. | author = K. Isobe, et al. | journal =  J Biosci Bioeng | date = 2006 Jan | volume = 101 | issue = 1 | pages = 73-6 | doi = 10.1263/jbb.101.73 <!--Retrieved from CrossRef by DOI bot-->}}</ref>  
=== Acatalasia ===
[[Acatalasia]] is a condition caused by homozygous mutations in CAT, resulting in a lack of catalase. Symptoms are mild and include oral ulcers. A heterozygous CAT mutation results in lower, but still present catalase.<ref>{{cite web |title=OMIM Entry            - # 614097 - ACATALASEMIA |url=http://www.omim.org/entry/614097 |website=www.omim.org |language=en-us}}</ref>


Very few [[aerobic microorganisms]] are known that do not use catalase. [http://madsci.org/posts/archives/jun99/929507203.Gb.r.html]. ''Streptococcus'' species are an example of aerobic bacteria that do not possess catalase. Catalase has also been observed in some [[anaerobic]] [[microorganisms]], such as [[Methanosarcina barkeri]].<ref>{{cite journal | doi = 10.1099/mic.0.28542-0 | title = The catalase and superoxide dismutase genes are transcriptionally up-regulated upon oxidative stress in the strictly anaerobic archaeon Methanosarcina barkeri. | author = Andrei Brioukhanov, Alexander Netrusov, and Rik Eggen. | journal = [[Microbiology (journal)|Microbiology]] | volume = 152 | pages = 1671 - 1677 | year = 2006}}</ref>
=== Gray hair ===
Low levels of catalase may play a role in the [[Human hair color#Gray and white hair|graying]] process of human hair. Hydrogen peroxide is naturally produced by the body and broken down by catalase. If catalase levels decline, hydrogen peroxide cannot be broken down so well. The hydrogen peroxide interferes with the production of [[melanin]], the pigment that gives hair its color.<ref name="ScienceDaily_Grey_Hair">{{cite web | url = https://www.sciencedaily.com/releases/2009/02/090223131123.htm | title = Why Hair Turns Gray Is No Longer A Gray Area: Our Hair Bleaches Itself As We Grow Older | date = 2009-02-24 | work = Science News | publisher = ScienceDaily | accessdate = 2009-03-01}}</ref><ref name="pmid19237503">{{cite journal | vauthors = Wood JM, Decker H, Hartmann H, Chavan B, Rokos H, Spencer JD, Hasse S, Thornton MJ, Shalbaf M, Paus R, Schallreuter KU | title = Senile hair graying: H2O2-mediated oxidative stress affects human hair color by blunting methionine sulfoxide repair | journal = FASEB Journal | volume = 23 | issue = 7 | pages = 2065–75 | date = July 2009 | pmid = 19237503 | doi = 10.1096/fj.08-125435 }}</ref>


==Human applications==
== Interactions ==
[[Image:Hydrogen-peroxide-2D.png|left|thumb|Hydrogen peroxide]]
Catalase is used in the food industry for removing [[hydrogen peroxide]] from [[milk]] prior to [[cheese production]].[http://www.worthington-biochem.com/CTL/default.html] Another use is in [[food wrappers]], where it prevents food from [[oxidation|oxidizing]].[http://madsci.org/posts/archives/mar99/921636249.Gb.r.html] Catalase is also used in the [[textile]] industry, removing hydrogen peroxide from fabrics to make sure the material is peroxide-free.[http://www.p2pays.org/ref/11/10842.htm] A minor use is in [[contact lens]] hygiene - a few lens-cleaning products [[disinfection|disinfect]] the lens using a hydrogen peroxide solution; a solution containing catalase is then used to decompose the hydrogen peroxide before the lens is used again.<ref>{{US patent|5521091}}</ref> Recently, catalase has also begun to be used in the aesthetics industry. Several mask treatments combine the enzyme with hydrogen peroxide on the face with the intent of increasing cellular oxygenation in the upper layers of the [[Epidermis (skin)|epidermis]].
{{-}}


==Pathology==
Catalase has been shown to [[Protein-protein interaction|interact]] with the ''[[ABL2]]''<ref name="pmid12777400">{{cite journal | vauthors = Cao C, Leng Y, Kufe D | title = Catalase activity is regulated by c-Abl and Arg in the oxidative stress response | journal = The Journal of Biological Chemistry | volume = 278 | issue = 32 | pages = 29667–75 | date = August 2003 | pmid = 12777400 | doi = 10.1074/jbc.M301292200 }}</ref> and ''[[Abl gene|Abl]]'' genes.<ref name=pmid12777400/>  Infection with the [[murine leukemia virus]] causes catalase activity to decline in the lungs, heart and kidneys of mice.  Conversely, dietary fish oil increased catalase activity in the heart, and kidneys of mice.<ref>{{cite journal |doi=10.1016/S0271-5317(00)00214-1 |title=Effects of dietary fish oil on tissue glutathione and antioxidant defense enzymes in mice with murine aids |journal=Nutrition Research |volume=20 |issue=9 |pages=1287–99 |year=2000 | vauthors = Xi S, Chen LH }}</ref>
The [[peroxisomal disorder]] [[acatalasia]] is due to a deficiency in the function of catalase.


== See also ==
== See also ==
* [[Enzyme kinetics]]
* [[Enzyme kinetics]]
* [[Peroxidases]]
* [[Glutathione peroxidase]]
* [[Superoxide dismutase]]</s>
* [[Peroxidase]]
 
* [[Superoxide dismutase]]
==References==
{{Reflist|2}}


==External links==
== References ==
* [http://genomics.senescence.info/genes/entry.php?hugo=CAT CAT] at the GenAge database.
{{Reflist|35em}}
* [http://www.seps.org/cvoracle/faq/catalase.html Catalase FAQ]
* [http://madsci.org/FAQs/catalase.html Catalase Enzymatics, Expression and Applications ''MadSci Network'']
* [http://www.tgw1916.net/movies.html Bacteria catalase test video]


== External links ==
* {{cite web | url = http://genomics.senescence.info/genes/entry.php?hugo=CAT | title = GenAge entry for CAT (Homo sapiens) | publisher = Human Ageing Genomic Resources | accessdate = 2009-03-05}}
* {{cite web | url = http://madsci.org/FAQs/catalase.html | title = Catalase | work = MadSci FAQ | publisher = madsci.org | accessdate = 2009-03-05}}
* {{cite web | url = http://www.tgw1916.net/video_pages/catalase.html | title = Catalase and oxidase test video | publisher = Regnvm Prokaryotae | accessdate = 2009-03-05}}
* {{cite web | url = http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.6 | title = EC 1.11.1.6 - catalase | publisher = Brenda: The Comprehensive Enzyme Information System| accessdate = 2009-03-05}}
* {{cite web|url=http://peroxibase.isb-sib.ch/ |title=PeroxiBase - The peroxidase database |publisher=[[Swiss Institute of Bioinformatics]] |accessdate=2009-03-05 |deadurl=yes |archiveurl=https://web.archive.org/web/20081013084336/http://peroxibase.isb-sib.ch/ |archivedate=2008-10-13 |df= }}
* {{cite web | url = http://microbeid.com/Methods/catalase.html | title = Catalase Procedure | publisher = MicrobeID.com | accessdate = 2009-04-22}}
* {{cite web | url = http://www.rcsb.org/pdb/101/motm.do?momID=57.html | title = Catalase Molecule of the Month | publisher = Protein Data Bank | accessdate = 2013-01-08 | deadurl = yes | archiveurl = https://web.archive.org/web/20130511202517/http://www.rcsb.org/pdb/101/motm.do?momID=57.html | archivedate = 2013-05-11 | df =  }}
{{Peroxisomal metabolism enzymes}}
{{Peroxidases}}
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{{Enzymes}}
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[[Category:EC 1.11.1]]
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[[Category:Hemoproteins]]
[[Category:Hemoproteins]]
[[Category:Enzymes]]
[[Category:Enzymes]]
 
[[Category:Catalysis]]
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[[ar:كتالاز]]
[[ca:Catalasa]]
[[cs:Kataláza]]
[[de:Katalase]]
[[es:Catalasa]]
[[eu:Katalasa]]
[[fr:Catalase]]
[[it:Catalasi]]
[[nl:Katalase]]
[[ja:カタラーゼ]]
[[pl:Katalaza]]
[[pt:Catalase]]
[[ru:Каталаза]]
[[sl:Katalaza]]
[[sr:Каталаза]]
[[sv:Katalas]]
[[uk:Каталаза]]
[[zh:过氧化氢酶]]
 
for systematic sequence analysis of catalases AND peroxidases
see http://peroxibase.isb-sib.ch/

Latest revision as of 18:30, 2 January 2019

Catalase
File:PDB 7cat EBI.jpg
Identifiers
SymbolCatalase
PfamPF00199
InterProIPR011614
PROSITEPDOC00395
SCOP7cat
SUPERFAMILY7cat
OPM superfamily370
OPM protein3e4w
CDDcd00328
Catalase
Identifiers
EC number1.11.1.6
CAS number9001-05-2
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Catalase is a common enzyme found in nearly all living organisms exposed to oxygen (such as bacteria, plants, and animals). It catalyzes the decomposition of hydrogen peroxide to water and oxygen.[1] It is a very important enzyme in protecting the cell from oxidative damage by reactive oxygen species (ROS). Likewise, catalase has one of the highest turnover numbers of all enzymes; one catalase molecule can convert millions of hydrogen peroxide molecules to water and oxygen each second.[2]

Catalase is a tetramer of four polypeptide chains, each over 500 amino acids long.[3] It contains four iron-containing heme groups that allow the enzyme to react with the hydrogen peroxide. The optimum pH for human catalase is approximately 7,[4] and has a fairly broad maximum: the rate of reaction does not change appreciably between pH 6.8 and 7.5.[5] The pH optimum for other catalases varies between 4 and 11 depending on the species.[6] The optimum temperature also varies by species.[7]

Structure

Human catalase forms a tetramer composed of four subunits, each of which can be conceptually divided into four domains.[8] The extensive core of each subunit is generated by an eight-stranded antiparallel b-barrel (b1-8), with nearest neighbor connectivity capped by b-barrel loops on one side and a9 loops on the other.[8] A helical domain at one face of the b-barrel is composed of four C-terminal helices (a16, a17, a18, and a19) and four helices derived from residues between b4 and b5 (a4, a5, a6, and a7).[8] Alternative splicing may result in different protein variants.

History

Catalase was not noticed until 1818 when Louis Jacques Thénard, who discovered H2O2 (hydrogen peroxide), suggested its breakdown is caused by an unknown substance. In 1900, Oscar Loew was the first to give it the name catalase, and found it in many plants and animals.[9] In 1937 catalase from beef liver was crystallised by James B. Sumner and Alexander Dounce[10] and the molecular weight was found in 1938.[11]

The amino acid sequence of bovine catalase was determined in 1969,[12] and the three-dimensional structure in 1981.[13]

Function

Reaction

2 H2O2 → 2 H2O + O2

The presence of catalase in a microbial or tissue sample can be demonstrated by adding hydrogen peroxide and observing the reaction. The production of oxygen can be seen by the formation of bubbles. This easy test, which can be seen with the naked eye, without the aid of instruments, is possible because catalase has a very high specific activity, which produces a detectable response, as well as the fact that one of the products is a gas.

Molecular mechanism

While the complete mechanism of catalase is not currently known,[14] the reaction is believed to occur in two stages:

H2O2 + Fe(III)-E → H2O + O=Fe(IV)-E(.+)
H2O2 + O=Fe(IV)-E(.+) → H2O + Fe(III)-E + O2[14]

Here Fe()-E represents the iron center of the heme group attached to the enzyme. Fe(IV)-E(.+) is a mesomeric form of Fe(V)-E, meaning the iron is not completely oxidized to +V, but receives some stabilising electron density from the heme ligand, which is then shown as a radical cation (.+).

As hydrogen peroxide enters the active site, it interacts with the amino acids Asn148 (asparagine at position 148) and His75, causing a proton (hydrogen ion) to transfer between the oxygen atoms. The free oxygen atom coordinates, freeing the newly formed water molecule and Fe(IV)=O. Fe(IV)=O reacts with a second hydrogen peroxide molecule to reform Fe(III)-E and produce water and oxygen.[14] The reactivity of the iron center may be improved by the presence of the phenolate ligand of Tyr358 in the fifth coordination position, which can assist in the oxidation of the Fe(III) to Fe(IV). The efficiency of the reaction may also be improved by the interactions of His75 and Asn148 with reaction intermediates.[14] In general, the rate of the reaction can be determined by the Michaelis-Menten equation.[15]

Catalase can also catalyze the oxidation, by hydrogen peroxide, of various metabolites and toxins, including formaldehyde, formic acid, phenols, acetaldehyde and alcohols. It does so according to the following reaction:

H2O2 + H2R → 2H2O + R

The exact mechanism of this reaction is not known.

Any heavy metal ion (such as copper cations in copper(II) sulfate) can act as a noncompetitive inhibitor of catalase. Furthermore, the poison cyanide is a noncompetitive inhibitor[16] of catalase at high concentrations of hydrogen peroxide.[17] Arsenate acts as an activator.[18] Three-dimensional protein structures of the peroxidated catalase intermediates are available at the Protein Data Bank.

Cellular role

Hydrogen peroxide is a harmful byproduct of many normal metabolic processes; to prevent damage to cells and tissues, it must be quickly converted into other, less dangerous substances. To this end, catalase is frequently used by cells to rapidly catalyze the decomposition of hydrogen peroxide into less-reactive gaseous oxygen and water molecules.[19]

Mice genetically engineered to lack catalase are initially phenotypically normal.,[20] however, catalase deficiency in mice may increase the likelihood of developing obesity, fatty liver,[21] and type 2 diabetes.[22] Some humans have very low levels of catalase (acatalasia), yet show few ill effects.

The increased oxidative stress that occurs with aging in mice is alleviated by over-expression of catalase.[23] Over-expressing mice do not exhibit the age-associated loss of spermatozoa, testicular germ and Sertoli cells seen in wild-type mice. Oxidative stress in wild-type mice ordinarily induces oxidative DNA damage (measured as 8-oxodG) in sperm with aging, but these damages are significantly reduced in aged catalase over-expressing mice.[23] Furthermore, these over-expressing mice show no decrease in age-dependent number of pups per litter. Overexpression of catalase targeted to mitochondria extends the lifespan of mice.[24]

Catalase is usually located in a cellular organelle called the peroxisome.[25] Peroxisomes in plant cells are involved in photorespiration (the use of oxygen and production of carbon dioxide) and symbiotic nitrogen fixation (the breaking apart of diatomic nitrogen (N2) to reactive nitrogen atoms). Hydrogen peroxide is used as a potent antimicrobial agent when cells are infected with a pathogen. Catalase-positive pathogens, such as Mycobacterium tuberculosis, Legionella pneumophila, and Campylobacter jejuni, make catalase to deactivate the peroxide radicals, thus allowing them to survive unharmed within the host.[26]

Like alcohol dehydrogenase, catalase converts ethanol to acetaldehyde, but it is unlikely that this reaction is physiologically significant.[27]

Distribution among organisms

The large majority of known organisms use catalase in every organ, with particularly high concentrations occurring in the liver in mammals.[28]Almost all aerobic microorganisms use catalase. It is also present in some anaerobic microorganisms, such as Methanosarcina barkeri.[29] Catalase is also universal among plants and occurs in most fungi.[30]

One unique use of catalase occurs in the bombardier beetle. This beetle has two sets of liquids that are stored separately in two paired glands. The larger of the pair, the storage chamber or reservoir, contains hydroquinones and hydrogen peroxide, while the smaller, the reaction chamber, contains catalases and peroxidases. To activate the noxious spray, the beetle mixes the contents of the two compartments, causing oxygen to be liberated from hydrogen peroxide. The oxygen oxidizes the hydroquinones and also acts as the propellant.[31] The oxidation reaction is very exothermic (ΔH = −202.8 kJ/mol) and rapidly heats the mixture to the boiling point.[32]

Long-lived queens of the termite Reticulitermes speratus have significantly lower oxidative damage to their DNA than non-reproductive individuals (workers and soldiers).[33] Queens have more than two times higher catalase activity and seven times higher expression levels of the catalase gene RsCAT1 than workers.[33] It appears that the efficient antioxidant capability of termite queens can partly explain how they attain longer life.

Catalase enzymes from various species have vastly differing optimum temperatures. Poikilothermic animals typically have catalases with optimum temperatures in the range of 15-25 °C, while mammalian or avian catalases might have optimum temperatures above 35 °C,[34][35] and catalases from plants vary depending on their growth habit.[34] In contrast, catalase isolated from the hyperthermophile archaeon Pyrobaculum calidifontis has a temperature optimum of 90 °C.[36]

Clinical significance and application

Hydrogen peroxide

Catalase is used in the food industry for removing hydrogen peroxide from milk prior to cheese production.[37] Another use is in food wrappers where it prevents food from oxidizing.[38] Catalase is also used in the textile industry, removing hydrogen peroxide from fabrics to make sure the material is peroxide-free.[39]

A minor use is in contact lens hygiene – a few lens-cleaning products disinfect the lens using a hydrogen peroxide solution; a solution containing catalase is then used to decompose the hydrogen peroxide before the lens is used again.[40]

Bacterial identification (catalase test)

File:Catalase reaction.jpg
Positive catalase reaction

The catalase test is one of the three main tests used by microbiologists to identify species of bacteria. If the bacteria possess catalase (i.e., are catalase-positive), when a small amount of bacterial isolate is added to hydrogen peroxide, bubbles of oxygen are observed. The catalase test is done by placing a drop of hydrogen peroxide on a microscope slide. An applicator stick is touched to the colony, and the tip is then smeared onto the hydrogen peroxide drop.

While the catalase test alone cannot identify a particular organism, it can aid identification when combined with other tests such as antibiotic resistance. The presence of catalase in bacterial cells depends on both the growth condition and the medium used to grow the cells.

Capillary tubes may also be used. A small sample of bacteria is collected on the end of the capillary tube, without blocking the tube, to avoid false negative results. The opposite end is then dipped into hydrogen peroxide, which is drawn into the tube through capillary action, and turned upside down, so that the bacterial points downwards. The hand holding the tube is then tapped on the bench, moving the hydrogen peroxide down until it touches the bacteria. If bubbles form on contact, this indicates a positive catalase result. This test can detect catalase-positive bacteria at concentrations above about 105 cells/mL,[44] and is simple to use.

Bacterial virulence

Neutrophils and other phagocytes use peroxide to kill bacteria. The enzyme NADPH oxidase generates superoxide within the phagosome, which is converted via hydrogen peroxide to other oxidising substances like hypochlorous acid which kill phagocytosed pathogens.[45] In individuals with chronic granulomatous disease (CGD) there is a defect in producing peroxide via mutations in phagocyte oxidases such as myeloperoxidase.[46] Normal cellular metabolism will still produce a small amount of peroxide and this peroxide can be used to produce hypochlorous acid to eradicate the bacterial infection. However, if individuals with CGD are infected with catalase-positive bacteria, the bacterial catalase can destroy the excess peroxide before it can be used to produce other oxidising substances. In these individuals the pathogen survives and becomes a chronic infection. This chronic infection is typically surrounded by macrophages in an attempt to isolate the infection. This wall of macrophages surrounding a pathogen is called a granuloma. Many bacteria are catalase positive, but some are better catalase-producers than others. The mnemonic "cats Need PLACESS to Belch their Hairballs" can be used to memorise the catalase-positive bacteria: nocardia, pseudomonas, listeria, aspergillus, candida, E. coli, staphylococcus, serratia, B. cepacia and H. pylori.[47]

Acatalasia

Acatalasia is a condition caused by homozygous mutations in CAT, resulting in a lack of catalase. Symptoms are mild and include oral ulcers. A heterozygous CAT mutation results in lower, but still present catalase.[48]

Gray hair

Low levels of catalase may play a role in the graying process of human hair. Hydrogen peroxide is naturally produced by the body and broken down by catalase. If catalase levels decline, hydrogen peroxide cannot be broken down so well. The hydrogen peroxide interferes with the production of melanin, the pigment that gives hair its color.[49][50]

Interactions

Catalase has been shown to interact with the ABL2[51] and Abl genes.[51] Infection with the murine leukemia virus causes catalase activity to decline in the lungs, heart and kidneys of mice. Conversely, dietary fish oil increased catalase activity in the heart, and kidneys of mice.[52]

See also

References

  1. ↑ Chelikani P, Fita I, Loewen PC (January 2004). "Diversity of structures and properties among catalases". Cellular and Molecular Life Sciences. 61 (2): 192–208. doi:10.1007/s00018-003-3206-5. PMID 14745498.
  2. ↑ Goodsell DS (2004-09-01). "Catalase". Molecule of the Month. RCSB Protein Data Bank. Retrieved 2016-08-23.
  3. ↑ Boon EM, Downs A, Marcey D. "Catalase: H2O2: H2O2 Oxidoreductase". Catalase Structural Tutorial Text. Retrieved 2007-02-11.
  4. ↑ Maehly AC, Chance B (1954). "The assay of catalases and peroxidases". Methods of Biochemical Analysis. Methods of Biochemical Analysis. 1: 357–424. doi:10.1002/9780470110171.ch14. ISBN 978-0-470-11017-1. PMID 13193536.
  5. ↑ Aebi H (1984). "Catalase in vitro". Methods in Enzymology. Methods in Enzymology. 105: 121–6. doi:10.1016/S0076-6879(84)05016-3. ISBN 978-0-12-182005-3. PMID 6727660.
  6. ↑ "EC 1.11.1.6 - catalase". BRENDA: The Comprehensive Enzyme Information System. Department of Bioinformatics and Biochemistry, Technische Universität Braunschweig. Retrieved 2009-05-26.
  7. ↑ Toner K, Sojka G, Ellis R. "A Quantitative Enzyme Study; CATALASE". bucknell.edu. Archived from the original on 2000-06-12. Retrieved 2007-02-11.
  8. ↑ 8.0 8.1 8.2 Putnam CD, Arvai AS, Bourne Y, Tainer JA (February 2000). "Active and inhibited human catalase structures: ligand and NADPH binding and catalytic mechanism". Journal of Molecular Biology. 296 (1): 295–309. doi:10.1006/jmbi.1999.3458. PMID 10656833.
  9. ↑ Loew O (May 1900). "A New Enzyme of General Occurrence in Organisms". Science. 11 (279): 701–2. Bibcode:1900Sci....11..701L. doi:10.1126/science.11.279.701. JSTOR 1625707. PMID 17751716.
  10. ↑ Sumner JB, Dounce AL (April 1937). "Crystalline Catalase". Science. 85 (2206): 366–7. Bibcode:1937Sci....85..366S. doi:10.1126/science.85.2206.366. PMID 17776781.
  11. ↑ Sumner JB, Gralén N (March 1938). "The Molecular Weight Of Crystalline Catalase". Science. 87 (2256): 284. Bibcode:1938Sci....87..284S. doi:10.1126/science.87.2256.284. PMID 17831682.
  12. ↑ Schroeder WA, Shelton JR, Shelton JB, Robberson B, Apell G (May 1969). "The amino acid sequence of bovine liver catalase: a preliminary report". Archives of Biochemistry and Biophysics. 131 (2): 653–5. doi:10.1016/0003-9861(69)90441-X. PMID 4892021.
  13. ↑ Murthy MR, Reid TJ, Sicignano A, Tanaka N, Rossmann MG (October 1981). "Structure of beef liver catalase". Journal of Molecular Biology. 152 (2): 465–99. doi:10.1016/0022-2836(81)90254-0. PMID 7328661.
  14. ↑ 14.0 14.1 14.2 14.3 Boon EM, Downs A, Marcey D. "Proposed Mechanism of Catalase". Catalase: H2O2: H2O2 Oxidoreductase: Catalase Structural Tutorial. Retrieved 2007-02-11.
  15. ↑ Maass E (1998-07-19). "How does the concentration of hydrogen peroxide affect the reaction". MadSci Network. Retrieved 2009-03-02.
  16. ↑ Nonstationary Inhibition of Enzyme Action. The Cyanide Inhibition of Catalase
  17. ↑ Ogura Y, Yamazaki I (August 1983). "Steady-state kinetics of the catalase reaction in the presence of cyanide". Journal of Biochemistry. 94 (2): 403–8. doi:10.1093/oxfordjournals.jbchem.a134369. PMID 6630165.
  18. ↑ Kertulis-Tartar GM, Rathinasabapathi B, Ma LQ (October 2009). "Characterization of glutathione reductase and catalase in the fronds of two Pteris ferns upon arsenic exposure". Plant Physiology and Biochemistry. 47 (10): 960–5. doi:10.1016/j.plaphy.2009.05.009. PMID 19574057.
  19. ↑ Gaetani GF, Ferraris AM, Rolfo M, Mangerini R, Arena S, Kirkman HN (February 1996). "Predominant role of catalase in the disposal of hydrogen peroxide within human erythrocytes". Blood. 87 (4): 1595–9. PMID 8608252.
  20. ↑ Ho YS, Xiong Y, Ma W, Spector A, Ho DS (July 2004). "Mice lacking catalase develop normally but show differential sensitivity to oxidant tissue injury". The Journal of Biological Chemistry. 279 (31): 32804–12. doi:10.1074/jbc.M404800200. PMID 15178682.
  21. ↑ Heit C, Marshall S, Singh S, Yu X, Charkoftaki G, Zhao H, Orlicky DJ, Fritz KS, Thompson DC, Vasiliou V (2017). "Catalase deletion promotes prediabetic phenotype in mice". Free Radical Biology & Medicine. 103: 48–56. doi:10.1016/j.freeradbiomed.2016.12.011. PMC 5513671. PMID 27939935.
  22. ↑ Góth L, Nagy T (2012). "Acatalasemia and diabetes mellitus". Archives of Biochemistry and Biophysics. 525 (2): 195–200. doi:10.1016/j.abb.2012.02.005. PMID 22365890.
  23. ↑ 23.0 23.1 Selvaratnam J, Robaire B (November 2016). "Overexpression of catalase in mice reduces age-related oxidative stress and maintains sperm production". Exp. Gerontol. 84: 12–20. doi:10.1016/j.exger.2016.08.012. PMID 27575890.
  24. ↑ Schriner SE, Linford NJ, Martin GM, Treuting P, Ogburn CE, Emond M, Coskun PE, Ladiges W, Wolf N, Van Remmen H, Wallace DC, Rabinovitch PS (June 2005). "Extension of murine life span by overexpression of catalase targeted to mitochondria". Science. 308 (5730): 1909–11. Bibcode:2005Sci...308.1909S. doi:10.1126/science.1106653. PMID 15879174.
  25. ↑ Alberts B, Johnson A, Lewis J, Raff M, Roberts K, Walter P (2002). "Peroxisomes". Molecular Biology of the Cell (4th ed.). New York: Garland Science. ISBN 978-0-8153-3218-3.
  26. ↑ Srinivasa Rao PS, Yamada Y, Leung KY (September 2003). "A major catalase (KatB) that is required for resistance to H2O2 and phagocyte-mediated killing in Edwardsiella tarda". Microbiology. 149 (Pt 9): 2635–44. doi:10.1099/mic.0.26478-0. PMID 12949187.
  27. ↑ Lieber, Charles S. (January 1997). "Ethanol metabolism, cirrhosis and alcoholism". Clinica Chimica Acta. 257 (1): 59–84. doi:10.1016/S0009-8981(96)06434-0.
  28. ↑ Ilyukha VA (2001). "Superoxide Dismutase and Catalase in the Organs of Mammals of Different Ecogenesis". Journal of Evolutionary Biochemistry and Physiology. 37 (3): 241–245. doi:10.1023/A:1012663105999.
  29. ↑ Brioukhanov AL, Netrusov AI, Eggen RI (June 2006). "The catalase and superoxide dismutase genes are transcriptionally up-regulated upon oxidative stress in the strictly anaerobic archaeon Methanosarcina barkeri". Microbiology. 152 (Pt 6): 1671–7. doi:10.1099/mic.0.28542-0. PMID 16735730.
  30. ↑ Hansberg W, Salas-Lizana R, Domínguez L (September 2012). "Fungal catalases: function, phylogenetic origin and structure". Archives of Biochemistry and Biophysics. 525 (2): 170–80. doi:10.1016/j.abb.2012.05.014. PMID 22698962.
  31. ↑ Eisner T, Aneshansley DJ (August 1999). "Spray aiming in the bombardier beetle: photographic evidence". Proceedings of the National Academy of Sciences of the United States of America. 96 (17): 9705–9. Bibcode:1999PNAS...96.9705E. doi:10.1073/pnas.96.17.9705. PMC 22274. PMID 10449758.
  32. ↑ Beheshti N, McIntosh AC (2006). "A biomimetic study of the explosive discharge of the bombardier beetle" (PDF). Int. Journal of Design & Nature. 1 (1): 1–9. Archived from the original (PDF) on 2011-07-26.
  33. ↑ 33.0 33.1 Tasaki E, Kobayashi K, Matsuura K, Iuchi Y (2017). "An Efficient Antioxidant System in a Long-Lived Termite Queen". PLoS ONE. 12 (1): e0167412. Bibcode:2017PLoSO..1267412T. doi:10.1371/journal.pone.0167412. PMC 5226355. PMID 28076409.
  34. ↑ 34.0 34.1 Mitsuda, Hisateru (1956-07-31). "Studies on Catalase" (PDF). Bulletin of the Institute for Chemical Research, Kyoto University. 34 (4): 165–192. Retrieved 27 September 2017.
  35. ↑ Akkuş Çetinus Ş, Nursevin Öztop H (June 2003). "Immobilization of catalase into chemically crosslinked chitosan beads". Enzyme and Microbial Technology. 32 (7): 889–894. doi:10.1016/S0141-0229(03)00065-6.
  36. ↑ Amo T, Atomi H, Imanaka T (June 2002). "Unique presence of a manganese catalase in a hyperthermophilic archaeon, Pyrobaculum calidifontis VA1". Journal of Bacteriology. 184 (12): 3305–12. doi:10.1128/JB.184.12.3305-3312.2002. PMC 135111. PMID 12029047.
  37. ↑ "Catalase". Worthington Enzyme Manual. Worthington Biochemical Corporation. Retrieved 2009-03-01.
  38. ↑ Hengge A (1999-03-16). "Re: how is catalase used in industry?". General Biology. MadSci Network. Retrieved 2009-03-01.
  39. ↑ "textile industry". Case study 228. International Cleaner Production Information Clearinghouse. Retrieved 2009-03-01.
  40. ↑ US patent 5521091, Cook JN, Worsley JL, "Compositions and method for destroying hydrogen peroxide on contact lens", issued 1996-05-28 
  41. ↑ Rollins DM (2000-08-01). "Bacterial Pathogen List". BSCI 424 Pathogenic Microbiology. University of Maryland. Retrieved 2009-03-01.
  42. ↑ Johnson M. "Catalase Production". Biochemical Tests. Mesa Community College. Archived from the original on 2008-12-11. Retrieved 2009-03-01.
  43. ↑ Fox A. "Streptococcus pneumoniae and Staphylococci". University of South Carolina. Retrieved 2009-03-01.
  44. ↑ Martin, A. M. (2012-12-06). Fisheries Processing: Biotechnological applications. Springer Science & Business Media. ISBN 9781461553038.
  45. ↑ Winterbourn, Christine C.; Kettle, Anthony J.; Hampton, Mark B. (2016-06-02). "Reactive Oxygen Species and Neutrophil Function". Annual Review of Biochemistry. 85 (1): 765–792. doi:10.1146/annurev-biochem-060815-014442. ISSN 0066-4154.
  46. ↑ Murphy, Patrick (2012-12-06). The Neutrophil. Springer Science & Business Media. ISBN 9781468474183.
  47. ↑ First aid for the USMLE step 1 2017 : a student-to-student guide. Le, Tao,, Bhushan, Vikas,, Sochat, Matthew,, Kallianos, Kimberly,, Chavda, Yash,, Zureick, Andrew H. (Andrew Harrison), 1991- (27th ed.). New York. ISBN 9781259837623. OCLC 986222844.
  48. ↑ "OMIM Entry - # 614097 - ACATALASEMIA". www.omim.org.
  49. ↑ "Why Hair Turns Gray Is No Longer A Gray Area: Our Hair Bleaches Itself As We Grow Older". Science News. ScienceDaily. 2009-02-24. Retrieved 2009-03-01.
  50. ↑ Wood JM, Decker H, Hartmann H, Chavan B, Rokos H, Spencer JD, Hasse S, Thornton MJ, Shalbaf M, Paus R, Schallreuter KU (July 2009). "Senile hair graying: H2O2-mediated oxidative stress affects human hair color by blunting methionine sulfoxide repair". FASEB Journal. 23 (7): 2065–75. doi:10.1096/fj.08-125435. PMID 19237503.
  51. ↑ 51.0 51.1 Cao C, Leng Y, Kufe D (August 2003). "Catalase activity is regulated by c-Abl and Arg in the oxidative stress response". The Journal of Biological Chemistry. 278 (32): 29667–75. doi:10.1074/jbc.M301292200. PMID 12777400.
  52. ↑ Xi S, Chen LH (2000). "Effects of dietary fish oil on tissue glutathione and antioxidant defense enzymes in mice with murine aids". Nutrition Research. 20 (9): 1287–99. doi:10.1016/S0271-5317(00)00214-1.

External links

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